Special Issue "Isothermal Titration Calorimetry"
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Physical Chemistry, Theoretical and Computational Chemistry".
Deadline for manuscript submissions: closed (31 May 2009).
Over the past decade Isothermal Titration Calorimetry (ITC) has been one of the fastest developing biophysical techniques, no longer constrained to specialist laboratories. Usage growth can be attributed to its near universality in studying biological macromolecular interactions coupled to its ease of use, adaptability and the quality of information that can be derived from a single titration.
ITC accurately determines the binding constant (K), reaction stoichiometry (n) and the thermodynamic contributions of enthalpy (DH) and entropy (TDS) changes to free energies of binding (DG). The combination of thermodynamic and structural information has dramatically enhanced our understanding of biological interactions in solution.
In this Special Issue, authors describe and analyse some of the most exciting new applications of ITC, including the use of ITC as a practical tool in enzyme assay development, studying small molecule-protein interactions in drug discovery and dissecting thermodynamic cooperativity in multivalent systems. This issue also demonstrates the application range of ITC with reviews describing interactions involving copolymers, surfactants, lipids and nucleic acid G-quadruplexes.
Tom L. Blundell
- isothermal titration calorimetry
- thermodynamic parameters of biochemical interactions
- binding affinity, enthalpy changes and binding stoichiometry measurements
- Gibbs energy
- entropy change